Proteomic View on Gluten Structure in Different Types of Flour and Bread Samples by Using Bottom Up Proteomics and Ft-Ir Spectroscopy

Abstract

In the current study, some proteomic methods containing 2D-PAGE and FT-IR techniques were performed to screen gliadin, the subunit of gluten protein, and transformation between α and β sheet forms of this protein was evaluated. The protein concentration of the samples varied between flour types and also cooked form of these samples. We focused on Amide A, Amide I and phosphorylated protein regions on the spectrums achieved by FT-IR. Gliadin structure was dramatically differed when the raw material was formed in baked form. While Amide A vibration which is related to N-H streching increased for the bread form of the white flour, Amide I which is related to C=O streching decreased when the raw material changed in the cooked form. It can be concluded that the type of flour used in bread production and the type of baking were effective on gluten structure and amount of the final product.